Assemblies
Multimeric state:
hetero octamer
Accessible surface area:
107221.57 Å2
Buried surface area:
34392.04 Å2
Dissociation area:
3,653.05
Å2
Dissociation energy (ΔGdiss):
-5.65
kcal/mol
Dissociation entropy (TΔSdiss):
39.96
kcal/mol
Symmetry number:
2
PDBe Complex ID:
PDB-CPX-112664
Macromolecules
Chains: A, E
Length: 958 amino acids
Theoretical weight: 104.59 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
Pfam:
Length: 958 amino acids
Theoretical weight: 104.59 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
- Canonical:
D5AQH0 (Residues: 1-958; Coverage: 100%)
Pfam:
- 2Fe-2S iron-sulfur cluster binding domain
- NADH-ubiquinone oxidoreductase-G iron-sulfur binding region
- 4Fe-4S dicluster domain
- Molybdopterin oxidoreductase Fe4S4 domain
- Molybdopterin oxidoreductase
- Molydopterin dinucleotide binding domain
- 2Fe-2S ferredoxin-type iron-sulfur binding domain
- 2Fe-2S ferredoxin-like superfamily
- NADH:ubiquinone oxidoreductase, subunit G, iron-sulphur binding
- 4Fe-4S ferredoxin-type, iron-sulphur binding domain
- 4Fe-4S ferredoxin, iron-sulphur binding, conserved site
- Molybdopterin oxidoreductase, 4Fe-4S domain
- Formate dehydrogenase, alpha subunit
- Formate dehydrogenase H, N-terminal
- Molybdopterin oxidoreductase
- Aspartate decarboxylase-like domain superfamily
- Molybdopterin dinucleotide-binding domain
- Molybdopterin oxidoreductase, prokaryotic, conserved site
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D5AQH0
Chains
Domains
Secondary structure
Flexibility predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: B, F
Length: 500 amino acids
Theoretical weight: 52.76 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
Pfam:
Length: 500 amino acids
Theoretical weight: 52.76 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
- Canonical:
D5AQH1 (Residues: 1-500; Coverage: 100%)
Pfam:
- Respiratory-chain NADH dehydrogenase 51 Kd subunit
- NADH-ubiquinone oxidoreductase-F iron-sulfur binding region
- NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain superfamily
- NADH-ubiquinone oxidoreductase 51kDa subunit, FMN-binding domain
- NADH:ubiquinone oxidoreductase, 51kDa subunit, conserved site
- NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain superfamily
- NADH-ubiquinone oxidoreductase 51kDa subunit, iron-sulphur binding domain
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D5AQH1
Chains
Domains
Secondary structure
Flexibility predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: C, G
Length: 150 amino acids
Theoretical weight: 15.6 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
Pfam: Thioredoxin-like [2Fe-2S] ferredoxin
InterPro:
Length: 150 amino acids
Theoretical weight: 15.6 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
- Canonical:
D5AQH2 (Residues: 1-150; Coverage: 100%)
Pfam: Thioredoxin-like [2Fe-2S] ferredoxin
InterPro:
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D5AQH2
Chains
Domains
Secondary structure
Flexibility predictions
Ligand binding sites
Interaction interfaces
Sequence conservation
Chains: D, H
Length: 71 amino acids
Theoretical weight: 7.39 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
Pfam: NADH-dependant formate dehydrogenase delta subunit FdsD
InterPro: Formate dehydrogenase, delta subunit
Length: 71 amino acids
Theoretical weight: 7.39 KDa
Source organism: Rhodobacter capsulatus
Expression system: Rhodobacter capsulatus
UniProt:
- Canonical:
D5AQG8 (Residues: 1-71; Coverage: 100%)
Pfam: NADH-dependant formate dehydrogenase delta subunit FdsD
InterPro: Formate dehydrogenase, delta subunit
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D5AQG8
Chains
Domains
Secondary structure
Flexibility predictions
Interaction interfaces
Sequence conservation